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Database: UniProt
Entry: A0A2C6DUU1_9GAMM
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ID   A0A2C6DUU1_9GAMM        Unreviewed;       371 AA.
AC   A0A2C6DUU1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase A {ECO:0000256|PIRNR:PIRNR019422};
DE            EC=4.2.2.n1 {ECO:0000256|PIRNR:PIRNR019422};
DE   AltName: Full=Murein hydrolase A {ECO:0000256|PIRNR:PIRNR019422};
GN   Name=mltA {ECO:0000313|EMBL:VFS53434.1};
GN   ORFNames=CRN84_23605 {ECO:0000313|EMBL:PHI32092.1}, NCTC12282_06493
GN   {ECO:0000313|EMBL:VFS53434.1};
OS   Budvicia aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Budvicia.
OX   NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI32092.1, ECO:0000313|Proteomes:UP000224974};
RN   [1] {ECO:0000313|EMBL:PHI32092.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI32092.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000224974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VFS53434.1, ECO:0000313|Proteomes:UP000373449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS53434.1,
RC   ECO:0000313|Proteomes:UP000373449};
RG   Pathogen Informatics;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division.
CC       {ECO:0000256|PIRNR:PIRNR019422}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001420,
CC         ECO:0000256|PIRNR:PIRNR019422};
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DR   EMBL; PDDX01000001; PHI32092.1; -; Genomic_DNA.
DR   EMBL; CAADJA010000002; VFS53434.1; -; Genomic_DNA.
DR   RefSeq; WP_029094402.1; NZ_PDDX01000001.1.
DR   AlphaFoldDB; A0A2C6DUU1; -.
DR   STRING; 1111728.GCA_000427805_01311; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000224974; Unassembled WGS sequence.
DR   Proteomes; UP000373449; Unassembled WGS sequence.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   CDD; cd22785; DPBB_MltA-like; 1.
DR   CDD; cd14668; mlta_B; 1.
DR   Gene3D; 2.40.240.50; Barwin-like endoglucanases; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|PIRNR:PIRNR019422};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224974}.
FT   DOMAIN          125..261
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   371 AA;  40943 MW;  F57E95EC876FBC9D CRC64;
     MKGCWAKYVL GGIIIALLAG CESRPTDRGQ QYKDGKLTHP FELVNNPNAK NKPVNGQDFA
     QQVSEISKVS PSLYAKHRDT YQAIFKWMVS GAEGAQLAQY KIDAYQMEGV DNFGNVQFTG
     YYTPVIHARH TKQGEFKYPL YSMPRKTKKM RRLPDRAGIY AGALDGLGLE LAYSNSLVDN
     FMMEVQGSAY VDFGDGTPLV FFAYSGKNGR AYHSVGKVLI DRNEVPREQM SMQAIKKWTE
     EHSESEVREL LEQNPSFVFF KPRHSAPVKG ASAVPLVAKA SVASDKTLIP PGTTILAEVP
     LLDNQGKFTG KYEMRLMVSL DVGGAIKGHH FDIYQGIGDD AGHAAGFYNH YGRVWVLSTP
     PDAASSLSVA K
//
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